1yxi
From Proteopedia
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| - | [[Image:1yxi.gif|left|200px]] | + | [[Image:1yxi.gif|left|200px]] |
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| - | '''R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase''' | + | {{Structure |
| + | |PDB= 1yxi |SIZE=350|CAPTION= <scene name='initialview01'>1yxi</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] | ||
| + | |GENE= FBP1, FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | ||
| + | }} | ||
| + | |||
| + | '''R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YXI is a [ | + | 1YXI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXI OCA]. |
==Reference== | ==Reference== | ||
| - | R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:[http:// | + | R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15767255 15767255] |
[[Category: Fructose-bisphosphatase]] | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: MG]] | [[Category: MG]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
| - | [[Category: 6-bisphosphatase; intermediate | + | [[Category: 6-bisphosphatase; intermediate state]] |
[[Category: glycolysis; gluconeogenesis; allosteric enzymes; fructose-1]] | [[Category: glycolysis; gluconeogenesis; allosteric enzymes; fructose-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:46 2008'' |
Revision as of 13:28, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | FBP1, FBP (Sus scrofa) | ||||||
| Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase
Overview
AMP transforms fructose-1,6-bisphosphatase from its active R-state to its inactive T-state; however, the mechanism of that transformation is poorly understood. The mutation of Ala(54) to leucine destabilizes the T-state of fructose-1,6-bisphosphatase. The mutant enzyme retains wild-type levels of activity, but the concentration of AMP that causes 50% inhibition increases 50-fold. In the absence of AMP, the Leu(54) enzyme adopts an R-state conformation nearly identical to that of the wild-type enzyme. The mutant enzyme, however, grows in two crystal forms in the presence of saturating AMP. In one form, the AMP-bound tetramer is in a T-like conformation, whereas in the other form, the AMP-bound tetramer is in a R-like conformation. The latter reveals conformational changes in two helices due to the binding of AMP. Helix H1 moves toward the center of the tetramer and displaces Ile(10) from a hydrophobic pocket. The displacement of Ile(10) exposes a hydrophobic surface critical to interactions that stabilize the T-state. Helix H2 moves away from the center of the tetramer, breaking hydrogen bonds with a buried loop (residues 187-195) in an adjacent subunit. The same hydrogen bonds reform but only after the quaternary transition to the T-state. Proposed here is a model that accounts for the quaternary transition and cooperativity in the inhibition of catalysis by AMP.
About this Structure
1YXI is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:15767255
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